Glutamate 5-kinase
     (GK)
     (EC 2.7.2.11)
     (Gamma-glutamyl kinase)
Gamma-glutamyl phosphate reductase
     (GPR)
     (EC 1.2.1.41)
     (Glutamate-5-semialdehyde dehydrogenase)
     (Glutamyl-gamma-semialdehyde dehydrogenase)

Gene name

None

From

Vigna aconitifolia (Mothbean)

[TaxID: 3918]

Taxonomy

Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons; rosids; eurosids I; Fabales; Fabaceae; Papilionoideae; Phaseoleae; Vigna.

Protein existence

2: Evidence at transcript level;

References

[1]

NUCLEOTIDE SEQUENCE [MRNA].
PubMed=1384052 [NCBI, ExPASy, EBI, Israel, Japan]
Hu C.-A.A., Delauney A.J., Verma D.P.S.;
"A bifunctional enzyme (delta 1-pyrroline-5-carboxylate synthetase) catalyzes the first two steps in proline biosynthesis in plants.";
Proc. Natl. Acad. Sci. U.S.A. 89:9354-9358(1992).

Comments

FUNCTION: P5CS plays a key role in proline biosynthesis, leading to osmoregulation in plants.
CATALYTIC ACTIVITY: ATP + L-glutamate = ADP + L-glutamate 5-phosphate.
CATALYTIC ACTIVITY: L-glutamate 5-semialdehyde + phosphate + NADP⁺ = L-glutamyl 5-phosphate + NADPH.
ENZYME REGULATION: Feedback regulated by proline.
PATHWAY: Amino-acid biosynthesis; L-proline biosynthesis; L-glutamate 5-semialdehyde from L-glutamate: step 1/2 .
PATHWAY: Amino-acid biosynthesis; L-proline biosynthesis; L-glutamate 5-semialdehyde from L-glutamate: step 2/2 .
TISSUE SPECIFICITY: Expressed at high levels in leaves and is inducible in roots subjected to salt stress.
SIMILARITY: In the N-terminal section; belongs to the glutamate 5-kinase family.
SIMILARITY: In the C-terminal section; belongs to the gamma-glutamyl phosphate reductase family.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

M92276; -; NOT_ANNOTATED_CDS; mRNA.

[EMBL / GenBank / DDBJ]

PIR

A46295; A46295.

3D structure databases

HSSP

Q9WYC9; 1O20. [HSSP ENTRY / PDB]

ModBase

P32296.

Family and domain databases

InterPro

IPR016163; Ald_DHase_C.
IPR016162; Ald_DHase_N.
IPR001048; Asp/Glu/Uridylate_kinase.
IPR000965; Gglut_pp_reduct.
IPR001057; Glu_5kinase.
IPR005766; P5_carboxy_syn.
IPR005715; ProB.
Graphical view of domain structure.

Gene3D

G3DSA:3.40.1160.10; Aa_kinase; 1.
G3DSA:3.40.309.10; Aldehyde_dehydrogenase_C; 1.
G3DSA:3.40.605.10; Aldehyde_dehydrogenase_N; 1.

Pfam

PF00696; AA_kinase; 1.
Pfam graphical view of domain structure.

PIRSF

PIRSF036429; P5C_syn; 1.

PRINTS

PR00474; GLU5KINASE.

TIGRFAMs

TIGR01092; P5CS; 1.
TIGR00407; proA; 1.
TIGR01027; proB; 1.

PROSITE

PS00902; GLUTAMATE_5_KINASE; 1.
PS01223; PROA; 1.

Other

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Amino-acid biosynthesis; Kinase; Multifunctional enzyme; NADP; Oxidoreductase; Proline biosynthesis; Transferase.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 671`	`671`	`Delta-1-pyrroline-5-carboxylate synthetase.`	`PRO_0000109778`
`REGION`	`1 297`	`297`	`Glutamate 5-kinase.`
`REGION`	`298 671`	`374`	`Gamma-glutamyl phosphate reductase.`

Sequence information

Length: 671 AA [This is the length of the unprocessed precursor]

Molecular weight: 73291 Da [This is the MW of the unprocessed precursor]

CRC64: 30BAE7AAF7ED1DA6 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MESAVDPSRG FMKDVKRVII KVGTAVVTRE EGRLAVGRLG ALCEQIKQLN SLGYDIILVS 

        70         80         90        100        110        120 
SGPVGIGRQR LRFRKLINSS FADLQKPQLE LDGKACAAVG QNSLMALYDT LFTQLDVTSA 

       130        140        150        160        170        180 
QLLVTDNDFR DKDFRKQLTE TVKSLLALKV IPVFNENDAV STRKAPYEDS SGIFWDNDSL 

       190        200        210        220        230        240 
SALLALELKA DLLVLLSDVE GLYSGPPSDP HSKLIYTYNK EKHQNEITFG DKSRVGRGGM 

       250        260        270        280        290        300 
TAKVKAAVHA AEAGIPVVIT SGFAPENIIN VLQGQRIGTL FHKDAHEWAQ VKEVDAREMA 

       310        320        330        340        350        360 
VAAGNVREGS RRYLQRKGNK ILLKIADALE ANEKIIRIEN EADVTAAQEA GYEKSLVARL 

       370        380        390        400        410        420 
ALKPGKIASL ANNMRIIANM EDPIGRVLKR TELSDGLILE KTSSPLGVLL IVFESRPDAL 

       430        440        450        460        470        480 
VQIASLAIRS GNGLLLKGGK EAKRSNAILH KVIIEAIPDN VGGKLIGLVT SREEIPELLK 

       490        500        510        520        530        540 
LDDVIDLVIP RGSNKLVSQI KSSTKIPVLG HADGICHVYV DKSANVEMAK RIVLDAKVDY 

       550        560        570        580        590        600 
PAACNAMETL LIHKDLIEKG WLKEIILDLR TEGVILYGGP VASSLLNIPQ AHSFHHEYSS 

       610        620        630        640        650        660 
LACTAEIVDD VYAAIDHINL YGSAHTDSIV AEDNEVANVF LRQVDSAAVF HNASTRFSDG 

       670 
ARFETRRRGW N

P32296 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools